Galanthus nivalis lectin, unlike most mannose-specific lectins, is not a metalloprotein and does not require Ca++ or Mn++ for binding.
Binding seems to be preferentially directed toward structures containing (α-1,3) mannose residues. Also in contrast to most mannose-binding lectins, GNL will not bind α-linked glucose. Reports indicate that this lectin binds rat and mouse IgM but not IgG. The only protein from human serum reported to bind to this lectin is α2-macroglobulin. GNL binds to many viral glycoproteins.
Biotinylated Galanthus nivalis lectin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.
|Unit Size||2 mg|
|Country of Manufacture||United States|
|Applications||Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Elispot, ELISAs, Glycobiology|
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